This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Molecular characterization of a gene that codifies for a disulfide reductase; the low molecular weight thiol compound and the enzyme that participate in the detoxifying mechanism of Entamoeba histolytica. We are looking for a thiol compound that substitutes in Entamoeba histolytica the absence of glutathione and disulfide reducing enzyme. By HPLC and using the fluorescent reagent monobromobimane we have been able to isolate two thiol compounds that have the characteristics of glutathione-spermidine and trypanothione [N1,N8,bis(L-gama-glutamyl-L-hemicysteinil-glycil)spermidine]. The mass spectrometry analysis will give a solid support to other results on the aminoacid composition obtained after acid hydrolisis of the two compounds isolated and purified from Entamoeba histolytica , as well as the results obtained by coelution with standards donated by the discoverer of these compounds from Crithidia fasciculata.
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